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PMID: 6273880 Published · ppublish English Journal Article

The dicyclohexylcarbodiimide-binding protein c of ATP synthase from Escherichia coli is not sufficient to express an efficient H+ conduction.

Friedl P, Bienhaus G, Hoppe J, Schairer HU

Abstract

Bacteriophage Mu was inserted into the unc genes of Escherichia coli. The resulting mutation AS12 had a polar effect on the unc operon: membranes of the mutant AS12 contained the dicyclohexylcarbodiimide-binding protein c and the protein a as sole subunits of the ATP synthase. It was shown by peptide mapping and amino acid analysis of the fragments that protein c from mutant AS12 was identical with the wild-type protein c. The absence of subunit b in mutant AS12 drastically lowered the H+ conduction dependent on the membrane-integrated moiety (F0) of the ATP synthase. This suggests that both subunits b and c are necessary for an efficient expression of H+ conduction.

MeSH Terms
ATP Synthetase Complexes Adenosine Diphosphate/metabolism Amino Acids/analysis Biological Transport, Active/drug effects Carrier Proteins/metabolism Cyanogen Bromide Dicyclohexylcarbodiimide/pharmacology Escherichia coli/enzymology Hydrogen-Ion Concentration Membrane Proteins/isolation & purification Multienzyme Complexes/metabolism Mutation Peptide Fragments/metabolism Phosphotransferases/metabolism
Chemicals
Amino Acids Carrier Proteins Membrane Proteins Multienzyme Complexes Peptide Fragments Dicyclohexylcarbodiimide Adenosine Diphosphate Phosphotransferases ATP Synthetase Complexes Cyanogen Bromide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Friedl P
Bienhaus G
Hoppe J
Schairer H U
References (31)
31 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1981-11-00
Pages
6643-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC349105
Subset
IM
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